Activation of the plasma membrane Na/H antiporter salt-overly-sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain

Francisco J. Quintero, Juliana Martínez-Atienza, Irene Villalta, Xingyu Jiang, Woeyeon Kim, Zhair Ali, Hiroaki Fujii, Imelda Mendoza, Daejin Yun, Jian-Kang Zhu, José Manuel Pardo

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194 Scopus citations

Abstract

The plasma membrane sodium/proton exchanger Salt-Overly-Sensitive 1 (SOS1) is a critical salt tolerance determinant in plants. The SOS2-SOS3 calcium-dependent protein kinase complex upregulates SOS1 activity, but the mechanistic details of this crucial event remain unresolved. Here we show that SOS1 is maintained in a resting state by a C-terminal auto-inhibitory domain that is the target of SOS2-SOS3. The auto-inhibitory domain interacts intramolecularly with an adjacent domain of SOS1 that is essential for activity. SOS1 is relieved from auto-inhibition upon phosphorylation of the auto-inhibitory domain by SOS2-SOS3. Mutation of the SOS2 phosphorylation and recognition site impeded the activation of SOS1 in vivo and in vitro. Additional amino acid residues critically important for SOS1 activity and regulation were identified in a genetic screen for hypermorphic alleles.
Original languageEnglish (US)
Pages (from-to)2611-2616
Number of pages6
JournalProceedings of the National Academy of Sciences
Volume108
Issue number6
DOIs
StatePublished - Jan 24 2011

ASJC Scopus subject areas

  • General

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